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PDBe Entry: 1ijh view

CHOLESTEROL OXIDASE FROM STREPTOMYCES ASN485LEU MUTANT
Summary
Header OXIDOREDUCTASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.53 Å, R-factor: 16.55%, Free R-factor: 21.27%, Spacegroup: P 1 21 1
Released 28/12/2001, deposition: 26/04/2001, last revision: 24/02/2009
Authors Vrielink, A.search; Lario, P.I.search
Primary citation The presence of a hydrogen bond between asparagine 485 and the pi system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidase.
BIOCHEMISTRYsearch vol:40, pag:13779-13787 (2001) [PubMed ID 11705367 ]search
Keywords FLAVOENZYMEsearch, STEROID METABOLISMsearch, OXIDOREDUCTASEsearch
EC 1.1.3.6 ExPASy BRENDA search (A)
Organism Streptomyces sp. 1931search(A)
UniProt Cholesterol oxidase precursor (EC 1.1.3.6) (CHOD) P12676search (A)
Solvent A
Related entries 1b4v, 1b8s, 1cbo, 1cc2
Polymers
Id Name Type UniProt Residues Observed
A CHOLESTEROL OXIDASE Protein P12676 (CHOD_STRS0)search
504 98%
Heterogens
Id Name Ligands
A FLAVIN-ADENINE DINUCLEOTIDE FAD search
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